September 26, 1995Biochemistry

Structural Basis for Actomyosin Chemomechanical Transduction by Non-Nucleoside Triphosphate Analogs

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Population

In vitro model using myosin subfragment 1 (S1) and actoS1

Comparison

Methylated 2-[amino]ethyl triphosphate vs Non-methylated dNOTP and ATP

Design

Preclinical

Authors

DGDamodaragounder GopalCase Western Reserve University ABAndrey A. BobkovSanford Burnham Prebys Medical Discovery Institute JSJames P. SchwonekUniversity School

Discussion

Member takes

Implication

Methylation disrupts myosin nucleotide binding in vitro; leaves open whether adenine modifications can guide cardiac myosin modulator development.

Structured PICO

Population

In vitro model using myosin subfragment 1 (S1) and actoS1

Intervention

Methylated 2-[(2,4-dinitrophenyl)amino]ethyl triphosphate (MdNOTP)

Comparator

Non-methylated dNOTP and ATP

Outcome

Rate of hydrolysis and ability to support actin sliding in an in vitro motility assaysurrogate

Methylation of dNOTP prevents specific interaction with myosin S1 in the adenine binding region, abolishing its ability to support actin sliding and providing insights into actomyosin chemomechanical transduction.

Cite This Study

Gopal et al. (1995) studied this question.

synapsesocial.com/papers/6a22fdd8c650520b07cb1fa1 https://doi.org/10.1021/bi00038a011

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Implication

Methylation disrupts myosin nucleotide binding in vitro; leaves open whether adenine modifications can guide cardiac myosin modulator development.

Structural Basis for Actomyosin Chemomechanical Transduction by Non-Nucleoside Triphosphate Analogs

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Structural Basis for Actomyosin Chemomechanical Transduction by Non-Nucleoside Triphosphate Analogs

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider